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. Author manuscript; available in PMC: 2008 Oct 19.
Published in final edited form as: J Biol Chem. 2007 Aug 16;282(42):30763–30775. doi: 10.1074/jbc.M704655200

TABLE 1. Purification of PPIP5K from rat brain.

The enzyme was purified as described in Figs. 3 and 4 and assayed under first-order conditions (k-1 is the first-order rate constant). The data for -fold purification and % recovery should be considered approximate because the enzyme co-purifies with an inhibitor (probably InsP6; see “Results” for details). Purification parameters for the native gel electrophoresis experiment are not available as the protein concentration in each gel slice was not determined.

Protein Volume Total activity Specific activity Purification Recovery
mg/ml ml k-1/mg/min k-1/mg/min -fold %
Supernatant 4.2 160 1,632 2.4 1 100
DEAE 1.2 193 1060 4.6 2 65
Heparin 0.075 60 653 145 60 40
Ni 0.1 9 870 967 402 53
Sucrose 0.04 3 429 3575 1490 26